The adhesive of the sea mussel Mytilus edulis has considerable appeal as a potential medical and dental restorative material. It sticks irreversibly to wet surfaces, has high bonding strengths and is nontoxic. In view of this, the following long-term goals have been defined: 1) to determine the mechanism of adhesion, 2) to develop techniques for adhesive production, and 3) to test its behavior and performance in animal and clinical studies. The specific aims of the present proposal are A. to complete the primary sequence determination of the adhesive protein by peptide mapping using thermolysin, chymotrypsin and pepsin for proteolysis; B. to determine what relationship the strength of mussel adhesion has to the extent of proline and tyrosine hydroxylation in the protein. To do this, mussels will be maintained in different regimes of water turbulence, followed by adhesive protein extraction, purification by HPLC and amino acid analysis particularly of 3-, 4-hydroxyprolines and DOPA; C. to provide direct evidence for adhesion of the polyphenolic protein to surfaces using a catalytic surface and incorporation of iodine-125. This method would provide for preferential labeling of proteins making contact at the surface. Such proteins can then be identified by autoradiography of electrophoretic separations of extracts.